Heterologous production, characterization and dye decolorization ability of a novel thermostable laccase isoenzyme from Trametes trogii BAFC 463

Laccases are multicopper polyphenol oxidases that are able to catalyze the oxidation of a wide range of phenolic compounds with the simultaneous reduction of O2 to H2O. Despite their promising industrial uses, feasible incorporation of laccases in harsh processes requires the bioprospecting and/or e...

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Detalles Bibliográficos
Autores principales:	Levin, Laura Noemi, Wirth, Sonia Alejandra
Publicado:	2016
Materias:	Acetosyringone Dye decolorization Pichia pastoris Thermostable laccase Trametes trogii Alkalinity C (programming language) Gene expression Laccases Pichia Pastoris Enzymes
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13595113_v51_n7_p895_Campos http://hdl.handle.net/20.500.12110/paper_13595113_v51_n7_p895_Campos
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_13595113_v51_n7_p895_Campos
record_format	dspace
spelling	paper:paper_13595113_v51_n7_p895_Campos2023-06-08T16:11:23Z Heterologous production, characterization and dye decolorization ability of a novel thermostable laccase isoenzyme from Trametes trogii BAFC 463 Levin, Laura Noemi Wirth, Sonia Alejandra Acetosyringone Dye decolorization Pichia pastoris Thermostable laccase Trametes trogii Alkalinity C (programming language) Gene expression Acetosyringone Dye decolorization Laccases Pichia Pastoris Trametes trogii Enzymes Laccases are multicopper polyphenol oxidases that are able to catalyze the oxidation of a wide range of phenolic compounds with the simultaneous reduction of O2 to H2O. Despite their promising industrial uses, feasible incorporation of laccases in harsh processes requires the bioprospecting and/or engineering of enzymes to be stable and active in acidic or alkaline pHs, high temperatures, oxidative conditions and tolerant to high salinity and/or organic solvents. Here we used a PCR-based screening to clone two novel laccase coding sequences from the white-rot basidiomycete Trametes trogii. Recombinant expression of lcc3 gene in Komagataella (=Pichia) pastoris showed that it encodes a thermo active and thermostable laccase with an optimum temperature of 50 °C and with a half-life of 45 min at 70 °C and a stability higher than 3 h at 60 °C. Furthermore, recombinant LCC3 was capable of decolorizing between 50% and 100% of indigoid, triarylmethane, azoic and anthraquinonic synthetic dyes in the presence of the natural redox mediator acetosyringone within 2 h of incubation at pH 6 and 70 °C. © 2016 Elsevier Ltd. Fil:Levin, L.N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Wirth, S.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2016 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13595113_v51_n7_p895_Campos http://hdl.handle.net/20.500.12110/paper_13595113_v51_n7_p895_Campos
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Acetosyringone Dye decolorization Pichia pastoris Thermostable laccase Trametes trogii Alkalinity C (programming language) Gene expression Acetosyringone Dye decolorization Laccases Pichia Pastoris Trametes trogii Enzymes
spellingShingle	Acetosyringone Dye decolorization Pichia pastoris Thermostable laccase Trametes trogii Alkalinity C (programming language) Gene expression Acetosyringone Dye decolorization Laccases Pichia Pastoris Trametes trogii Enzymes Levin, Laura Noemi Wirth, Sonia Alejandra Heterologous production, characterization and dye decolorization ability of a novel thermostable laccase isoenzyme from Trametes trogii BAFC 463
topic_facet	Acetosyringone Dye decolorization Pichia pastoris Thermostable laccase Trametes trogii Alkalinity C (programming language) Gene expression Acetosyringone Dye decolorization Laccases Pichia Pastoris Trametes trogii Enzymes
description	Laccases are multicopper polyphenol oxidases that are able to catalyze the oxidation of a wide range of phenolic compounds with the simultaneous reduction of O2 to H2O. Despite their promising industrial uses, feasible incorporation of laccases in harsh processes requires the bioprospecting and/or engineering of enzymes to be stable and active in acidic or alkaline pHs, high temperatures, oxidative conditions and tolerant to high salinity and/or organic solvents. Here we used a PCR-based screening to clone two novel laccase coding sequences from the white-rot basidiomycete Trametes trogii. Recombinant expression of lcc3 gene in Komagataella (=Pichia) pastoris showed that it encodes a thermo active and thermostable laccase with an optimum temperature of 50 °C and with a half-life of 45 min at 70 °C and a stability higher than 3 h at 60 °C. Furthermore, recombinant LCC3 was capable of decolorizing between 50% and 100% of indigoid, triarylmethane, azoic and anthraquinonic synthetic dyes in the presence of the natural redox mediator acetosyringone within 2 h of incubation at pH 6 and 70 °C. © 2016 Elsevier Ltd.
author	Levin, Laura Noemi Wirth, Sonia Alejandra
author_facet	Levin, Laura Noemi Wirth, Sonia Alejandra
author_sort	Levin, Laura Noemi
title	Heterologous production, characterization and dye decolorization ability of a novel thermostable laccase isoenzyme from Trametes trogii BAFC 463
title_short	Heterologous production, characterization and dye decolorization ability of a novel thermostable laccase isoenzyme from Trametes trogii BAFC 463
title_full	Heterologous production, characterization and dye decolorization ability of a novel thermostable laccase isoenzyme from Trametes trogii BAFC 463
title_fullStr	Heterologous production, characterization and dye decolorization ability of a novel thermostable laccase isoenzyme from Trametes trogii BAFC 463
title_full_unstemmed	Heterologous production, characterization and dye decolorization ability of a novel thermostable laccase isoenzyme from Trametes trogii BAFC 463
title_sort	heterologous production, characterization and dye decolorization ability of a novel thermostable laccase isoenzyme from trametes trogii bafc 463
publishDate	2016
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13595113_v51_n7_p895_Campos http://hdl.handle.net/20.500.12110/paper_13595113_v51_n7_p895_Campos
work_keys_str_mv	AT levinlauranoemi heterologousproductioncharacterizationanddyedecolorizationabilityofanovelthermostablelaccaseisoenzymefromtrametestrogiibafc463 AT wirthsoniaalejandra heterologousproductioncharacterizationanddyedecolorizationabilityofanovelthermostablelaccaseisoenzymefromtrametestrogiibafc463
_version_	1768545662571380736

Heterologous production, characterization and dye decolorization ability of a novel thermostable laccase isoenzyme from Trametes trogii BAFC 463

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